scholarly journals ISG56/IFIT1 is primarily responsible for interferon-induced changes to patterns of parainfluenza virus type 5 transcription and protein synthesis

2013 ◽  
Vol 94 (1) ◽  
pp. 59-68 ◽  
Author(s):  
J. Andrejeva ◽  
H. Norsted ◽  
M. Habjan ◽  
V. Thiel ◽  
S. Goodbourn ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Virus Type ◽  
Cellular Protein ◽  
Parainfluenza Virus ◽  
Hydroxyl Group ◽  
Virus Protein ◽  
Viral Mrnas ◽  
Tetratricopeptide Repeats ◽  
Virus Transcription

Interferon (IFN) induces an antiviral state in cells that results in alterations of the patterns and levels of parainfluenza virus type 5 (PIV5) transcripts and proteins. This study reports that IFN-stimulated gene 56/IFN-induced protein with tetratricopeptide repeats 1 (ISG56/IFIT1) is primarily responsible for these effects of IFN. It was shown that treating cells with IFN after infection resulted in an increase in virus transcription but an overall decrease in virus protein synthesis. As there was no obvious decrease in the overall levels of cellular protein synthesis in infected cells treated with IFN, these results suggested that ISG56/IFIT1 selectively inhibits the translation of viral mRNAs. This conclusion was supported by in vitro translation studies. Previous work has shown that ISG56/IFIT1 can restrict the replication of viruses lacking a 2′-O-methyltransferase activity, an enzyme that methylates the 2′-hydroxyl group of ribose sugars in the 5′-cap structures of mRNA. However, the data in the current study strongly suggested that PIV5 mRNAs are methylated at the 2′-hydroxyl group and thus that ISG56/IFIT1 selectively inhibits the translation of PIV5 mRNA by some as yet unrecognized mechanism. It was also shown that ISG56/IFIT1 is primarily responsible for the IFN-induced inhibition of PIV5.

scholarly journals Involvement of Actin Microfilaments in the Replication of Human Parainfluenza Virus Type 3

1998 ◽  
Vol 72 (4) ◽  
pp. 2655-2662 ◽  
Author(s):  
Sanhita Gupta ◽  
Bishnu P. De ◽  
Judith A. Drazba ◽  
Amiya K. Banerjee
Keyword(s):  
Virus Type ◽  
Parainfluenza Virus ◽  
Actin Microfilaments ◽  
Viral Mrnas ◽  
Polymeric Form ◽  
Genomic Rnas ◽  
Human Parainfluenza Virus ◽  
Type 3

ABSTRACT Several studies indicate that paramyxoviruses require a specific cellular factor(s) for transcription of their genomic RNAs. We previously reported that the cellular cytoskeletal protein actin, in its polymeric form, participates in the transcription of human parainfluenza virus type 3 (HPIV3) in vitro. In the present study, we investigated the role of the polymeric form of actin, i.e., the actin microfilaments of the cytoskeletal framework, in the reproduction of HPIV3 in vivo. Pulse-chase labeling analyses indicate that the viral nucleocapsid-associated proteins, NP and P, are present predominantly in the cytoskeletal framework during infection. By in situ hybridization, we found that viral mRNAs and genomic RNA were synthesized from the nucleocapsids that were bound to the cytoskeletal framework. Double immunofluorescent labeling and confocal microscopy of the cytoarchitecture revealed that the viral nucleocapsids are specifically localized on the actin microfilaments. Treatment of cells with the actin-depolymerizing agent, cytochalasin D, resulted in the inhibition of viral RNA synthesis and ribonucleoprotein accumulation. These results strongly suggest that actin microfilaments play an important role in the replication of HPIV3.

scholarly journals Amino acid regulation of synthesis of ribonucleic acid and protein in the liver of rats

1971 ◽  
Vol 124 (2) ◽  
pp. 385-392 ◽  
Author(s):  
R. W. Wannemacher ◽  
C. F. Wannemacher ◽  
M. B. Yatvin
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Free Amino Acids ◽  
Free Amino ◽  
Cellular Protein ◽  
Deficient Diet ◽  
Cellular Protein Content ◽  
Regulate Protein

Weanling (23-day-old) rats were fed on either a low-protein diet (6% casein) or a diet containing an adequate amount of protein (18% casein) for 28 days. Hepatic cells from animals fed on the deficient diet were characterized by markedly lower concentrations of protein and RNA in all cellular fractions as compared with cells from control rats. The bound rRNA fraction was decreased to the greatest degree, whereas the free ribosomal concentrations were only slightly less than in control animals. A good correlation was observed between the rate of hepatic protein synthesis in vivo and the cellular protein content of the liver. Rates of protein synthesis both in vivo and in vitro were directly correlated with the hepatic concentration of individual free amino acids that are essential for protein synthesis. The decreased protein-synthetic ability of the ribosomes from the liver of protein-deprived rats was related to a decrease in the number of active ribosomes and heavy polyribosomes. The lower ribosomal content of the hepatocytes was correlated with the decreased concentration of essential free amino acids. In the protein-deprived rats, the rate of accumulation of newly synthesized cytoplasmic rRNA was markedly decreased compared with control animals. From these results it was concluded that amino acids regulate protein synthesis (1) by affecting the number of ribosomes that actively synthesize protein and (2) by inhibiting the rate of synthesis of new ribosomes. Both of these processes may involve the synthesis of proteins with a rapid rate of turnover.

scholarly journals Detection, isolation, and in vitro characterization of porcine parainfluenza virus type 1 isolated from respiratory diagnostic specimens in swine

2019 ◽  
Vol 228 ◽  
pp. 219-225 ◽  
Author(s):  
Jie Yeun Park ◽  
Michael W. Welch ◽  
Karen M. Harmon ◽  
Jianqiang Zhang ◽  
Pablo E. Piñeyro ◽  
...  
Keyword(s):  
Virus Type ◽  
Parainfluenza Virus ◽  
In Vitro Characterization

scholarly journals In Vitro and In Vivo Interactions between the Hepatitis B Virus Protein P22 and the Cellular Protein gC1qR

2003 ◽  
Vol 77 (23) ◽  
pp. 12875-12880 ◽  
Author(s):  
S. Lainé ◽  
A. Thouard ◽  
J. Derancourt ◽  
M. Kress ◽  
D. Sitterlin ◽  
...  
Keyword(s):  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Matrix Protein ◽  
Cellular Protein ◽  
Virus Protein ◽  
B Virus ◽  
Immunofluorescence Studies ◽  
Cellular Partner

ABSTRACT gC1qR, a mitochondrial matrix protein, was identified as the main cellular partner of the hepatitis B virus P22 protein. We demonstrated by immunofluorescence studies that some P22 molecules were colocalized with the endogenous gC1qR in both the cytoplasm and the nucleus but never in the mitochondria. We also showed that the last 34 amino acids of P22 were involved in the association with gC1qR.

scholarly journals Parainfluenza Virus Type 1 Induces Epithelial IL-8 Production via p38-MAPK Signalling

2014 ◽  
Vol 2014 ◽  
pp. 1-12 ◽  
Author(s):  
Miguel Ángel Galván Morales ◽  
Carlos Cabello Gutiérrez ◽  
Fidencio Mejía Nepomuceno ◽  
Leticia Valle Peralta ◽  
Elba Valencia Maqueda ◽  
...  
Keyword(s):  
Viral Replication ◽  
Cell Lines ◽  
Virus Type ◽  
Molecular Mechanisms ◽  
Parainfluenza Virus ◽  
Kinase Activation ◽  
Mitogen Activated Protein ◽  
Human Parainfluenza Virus

Human parainfluenza virus type 1 (HPIV-1) is the most common cause of croup in infants. The aim of this study was to describe molecular mechanisms associated with IL-8 production during HPIV-1 infection and the role of viral replication in MAPK synthesis and activation. Anin vitromodel of HPIV-1 infection in the HEp-2 and A549 cell lines was used; a kinetic-based ELISA for IL-8 detection was also used, phosphorylation of the mitogen-activated protein kinases (MAPKs) was identified by Western blot analysis, and specific inhibitors for each kinase were used to identify which MAPK was involved. Inactivated viruses were used to assess whether viral replication is required for IL-8 production. Results revealed a gradual increase in IL-8 production at different selected times, when phosphorylation of MAPK was detected. The secretion of IL-8 in the two cell lines infected with the HPIV-1 is related to the phosphorylation of the MAPK as well as viral replication. Inhibition of p38 suppressed the secretion of IL-8 in the HEp-2 cells. No kinase activation was observed when viruses were inactivated.

scholarly journals HSP70–eIF4G Interaction Promotes Protein Synthesis and Cell Proliferation in Hepatocellular Carcinoma

Cancers ◽  
2020 ◽  
Vol 12 (8) ◽  
pp. 2262 ◽  
Author(s):  
Meng Wang ◽  
Kai Wei ◽  
Baifeng Qian ◽  
Svenja Feiler ◽  
Anastasia Lemekhova ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Cell Proliferation ◽  
Protein Synthesis ◽  
Critical Role ◽  
Cellular Protein ◽  
Hsp70 Expression ◽  
Tumor Escape ◽  
Cell Protection ◽  
Cellular Protein Synthesis

Hepatocellular carcinoma (HCC) is the third leading cause of cancer-related death worldwide and features various tumor escape mechanisms from treatment-induced stress. HSP70 plays a critical role in cell protection under stress. eIF4G physiologically regulates the formation of the protein-ribosomal complex and maintains cellular protein synthesis. However, the precise cooperation of both in HCC remains poorly understood. In this study, we demonstrate that HSP70 expression is positively correlated with eIF4G in tumor specimens from 25 HCC patients, in contrast to the adjacent non-tumorous tissues, and that both influence the survival of HCC patients. Mechanistically, this study indicates that HSP70 and eIF4G interact with each other in vitro. We further show that the HSP70–eIF4G interaction contributes to promoting cellular protein synthesis, enhancing cell proliferation, and inhibiting cell apoptosis. Collectively, this study reveals the pivotal role of HSP70–eIF4G interaction as an escape mechanism in HCC. Therefore, modulation of the HSP70–eIF4G interaction might be a potential novel therapeutic target of HCC treatment.

scholarly journals Magnetic Tracking of Protein Synthesis in Microfluidic Environments—Challenges and Perspectives

Nanomaterials ◽  
2019 ◽  
Vol 9 (4) ◽  
pp. 585 ◽  
Author(s):  
Wegener ◽  
Ennen ◽  
Walhorn ◽  
Anselmetti ◽  
Hütten ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Cell Biology ◽  
Ex Vivo ◽  
Microfluidic Devices ◽  
Cellular Protein ◽  
Fine Tuning ◽  
Superparamagnetic Particles ◽  
Magnetic Tracking ◽  
Selection Of

A novel technique to study protein synthesis is proposed that uses magnetic nanoparticles in combination with microfluidic devices to achieve new insights into translational regulation. Cellular protein synthesis is an energy-demanding process which is tightly controlled and is dependent on environmental and developmental requirements. Processivity and regulation of protein synthesis as part of the posttranslational nano-machinery has now moved back into the focus of cell biology, since it became apparent that multiple mechanisms are in place for fine-tuning of translation and conditional selection of transcripts. Recent methodological developments, such as ribosome foot printing, propel current research. Here we propose a strategy to open up a new field of labelling, separation, and analysis of specific polysomes using superparamagnetic particles following pharmacological arrest of translation during cell lysis and subsequent analysis. Translation occurs in polysomes, which are assemblies of specific transcripts, associated ribosomes, nascent polypeptides, and other factors. This supramolecular structure allows for unique approaches to selection of polysomes by targeting the specific transcript, ribosomes, or nascent polypeptides. Once labeled with functionalized superparamagnetic particles, such assemblies can be separated in microfluidic devices or magnetic ratchets and quantified. Insights into the dynamics of translation is obtained through quantifying large numbers of ribosomes along different locations of the polysome. Thus, an entire new concept for in vitro, ex vivo, and eventually single cell analysis will be realized and will allow for magnetic tracking of protein synthesis.

scholarly journals Role of Interferon in the Replication of Human Parainfluenza Virus Type 1 Wild Type and Mutant Viruses in Human Ciliated Airway Epithelium

2008 ◽  
Vol 82 (16) ◽  
pp. 8059-8070 ◽  
Author(s):  
Emmalene J. Bartlett ◽  
Margaret Hennessey ◽  
Mario H. Skiadopoulos ◽  
Alexander C. Schmidt ◽  
Peter L. Collins ◽  
...  
Keyword(s):  
Virus Type ◽  
Airway Epithelium ◽  
Parainfluenza Virus ◽  
Progeny Virus ◽  
Wild Type ◽  
Vaccine Candidates ◽  
C Proteins ◽  
Human Parainfluenza Virus

ABSTRACT Human parainfluenza virus type 1 (HPIV1) is a significant cause of pediatric respiratory disease in the upper and lower airways. An in vitro model of human ciliated airway epithelium (HAE), a useful tool for studying respiratory virus-host interactions, was used in this study to show that HPIV1 selectively infects ciliated cells within the HAE and that progeny virus is released from the apical surface with little apparent gross cytopathology. In HAE, type I interferon (IFN) is induced following infection with an HPIV1 mutant expressing defective C proteins with an F170S amino acid substitution, rHPIV1-CF170S, but not following infection with wild-type HPIV1. IFN induction coincided with a 100- to 1,000-fold reduction in virus titer, supporting the hypothesis that the HPIV1 C proteins are critical for the inhibition of the innate immune response. Two recently characterized live attenuated HPIV1 vaccine candidates expressing mutant C proteins were also evaluated in HAE. The vaccine candidates, rHPIV1-CR84G/Δ170HNT553ALY942A and rHPIV1-CR84G/Δ170HNT553ALΔ1710-11, which contain temperature-sensitive (ts) attenuating (att) and non-ts att mutations, were highly restricted in growth in HAE at permissive (32°C) and restrictive (37°C) temperatures. The viruses grew slightly better at 37°C than at 32°C, and rHPIV1-CR84G/Δ170HNT553ALY942A was less attenuated than rHPIV1-CR84G/Δ170HNT553ALΔ1710-11. The level of replication in HAE correlated with that previously observed for African green monkeys, suggesting that the HAE model has potential as a tool for the preclinical evaluation of HPIV1 vaccines, although how these in vitro data will correlate with vaccine virus replication in seronegative human subjects remains to be seen.

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